GenomeNet

Database: UniProt
Entry: A0A1S3VDI1_VIGRR
LinkDB: A0A1S3VDI1_VIGRR
Original site: A0A1S3VDI1_VIGRR 
ID   A0A1S3VDI1_VIGRR        Unreviewed;      1981 AA.
AC   A0A1S3VDI1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Chromatin modification-related protein EAF1 B isoform X1 {ECO:0000313|RefSeq:XP_014516267.1, ECO:0000313|RefSeq:XP_022642202.1};
GN   Name=LOC106774002 {ECO:0000313|RefSeq:XP_014516267.1,
GN   ECO:0000313|RefSeq:XP_022642202.1, ECO:0000313|RefSeq:XP_022642203.1,
GN   ECO:0000313|RefSeq:XP_022642204.1, ECO:0000313|RefSeq:XP_022642205.1,
GN   ECO:0000313|RefSeq:XP_022642206.1, ECO:0000313|RefSeq:XP_022642207.1,
GN   ECO:0000313|RefSeq:XP_022642208.1};
OS   Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014516267.1};
RN   [1] {ECO:0000313|RefSeq:XP_014516267.1, ECO:0000313|RefSeq:XP_022642202.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_014516267.1,
RC   ECO:0000313|RefSeq:XP_022642202.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_014516267.1; XM_014660781.2.
DR   RefSeq; XP_022642202.1; XM_022786481.1.
DR   RefSeq; XP_022642203.1; XM_022786482.1.
DR   RefSeq; XP_022642204.1; XM_022786483.1.
DR   RefSeq; XP_022642205.1; XM_022786484.1.
DR   RefSeq; XP_022642206.1; XM_022786485.1.
DR   RefSeq; XP_022642207.1; XM_022786486.1.
DR   RefSeq; XP_022642208.1; XM_022786487.1.
DR   STRING; 3916.A0A1S3VDI1; -.
DR   GeneID; 106774002; -.
DR   KEGG; vra:106774002; -.
DR   OrthoDB; 317967at2759; -.
DR   Proteomes; UP000087766; Chromosome 9.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:InterPro.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   CDD; cd00167; SANT; 1.
DR   InterPro; IPR044798; EAF1A/B.
DR   InterPro; IPR014012; HSA_dom.
DR   InterPro; IPR001005; SANT/Myb.
DR   PANTHER; PTHR46774; CHROMATIN MODIFICATION-RELATED PROTEIN EAF1 A-RELATED; 1.
DR   PANTHER; PTHR46774:SF3; CHROMATIN MODIFICATION-RELATED PROTEIN EAF1 A-RELATED; 1.
DR   Pfam; PF07529; HSA; 1.
DR   Pfam; PF13921; Myb_DNA-bind_6; 1.
DR   SMART; SM00573; HSA; 1.
DR   SMART; SM00717; SANT; 1.
DR   PROSITE; PS51204; HSA; 1.
DR   PROSITE; PS50090; MYB_LIKE; 1.
PE   4: Predicted;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087766}.
FT   DOMAIN          563..642
FT                   /note="HSA"
FT                   /evidence="ECO:0000259|PROSITE:PS51204"
FT   DOMAIN          1073..1125
FT                   /note="Myb-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50090"
FT   REGION          110..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          313..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1127..1153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1244..1314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1445..1507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1553..1653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1699..1770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1862..1894
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1912..1981
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..178
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1134..1153
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1255..1298
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1553..1617
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1628..1653
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1701..1770
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1912..1939
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1959..1981
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1981 AA;  216191 MW;  82FF41B6FB062023 CRC64;
     MNGYKSGSAL LVNAEVDSMG GVVDGGIGIG LKISPRRAAI EKAQAELREE YDAREERRRE
     LEFLEKGGNP LDFKSGNAAS VSVQSTSITD QPHEQFVTSE AKGSFALTAS PHADSVDSSA
     RPGAPLASEP NTADNLQLFD GENELPDTER RCLNRRNNIA VSEQSSQIDG SQNAKETEDS
     AIFRPYARRN RSRPIHGPRG PSREAKGLLL ETNNQKNPNL PTISKPEPSS LNCGIGAKSL
     TTNNTLNDEF VGIRDHQSTI GSASVPKDKL DITVNINLKE NRETLPSEDN TVQNPILMAT
     GEANVVELSK PIGVVNSDSP SHRPTTKAEN GPYDCQPNGF GNVEVDRKSV TNEGQNNIAR
     LGKKSFGLGS SCTQTSFGRH VNNDSDMCTN TKSVDANENT MEQTFTLENK LKSANCEFVK
     DRHKTKNGAI VSNEHDADCP DHSGSDNIIK AEEDFHINSS SMSNIKGVHN DSTTPKADTD
     TVLVDQSNSV KESSSERHQV PVDVSLSESP QTVLAEKVKS ATSDDQPCAM HNMKLVDKAR
     EDSILEEAQI IEAKRKRIAE LSLRSLPTQN HRKSHWGFVL EEMAWLANDF AQERLWKIAA
     AAQLGHRAAF TCMSRFEKLN KQLETRVLSH KIAKAVMQFW QSAELLLDND VENVDANEAI
     RDQRRNYNML PPETTTLLEG QNPVKRPALK VDAYALRFIK ANRSHGISSE AEAPTTPEKI
     FDSSTVDMSW DEHLNEESLF YEVSPTAVQT YRKAIESHFH HFENKLFQKT GSSIQEEIET
     SVYNTTAEFG SQENAYDEEE GENSTYYLPS VYEGNKSSKS AQKKHKILKS YTPRCSDAGA
     DLPYVHYTTG TQPSMMFGKR PPSLNVGSIP TKRMRTATRH RVVSPFTNIG TAQAQAKADA
     SSGDTNSFHD DQSTLHVGPL IQKGTEVESV ADFEKQLSYD SAETFLKTKK KKAKTLGSMY
     DQGWQLDYVV LNEQQRDQSK KRGDSHHFES IGSGGKATCL YGQHNGKKPK VMRPLDSPLD
     SIVPLSNSIP SPAASQMSNM SSPNKFIKII SGRDRGRKAK SLKTSAGQPG SGSPWSLFED
     QALVVLVHDM GPNWELVSDA INSALQIKCV FRKPKECKDR HKILMDRTTG DGADSAEDSG
     SSQSYPSTLP GIPKQGSARQ LFQRLQGPME EDTLKSHFEK IIKIGQKQHY LKNQIDNQDS
     KQVVAAHNSH VIALSLTSPN NLNGNLLTPL DLCEAEETNP DVPAVGYQGS HPGGLTLPHQ
     GSIQSTHPTS GVNSSLPGSS GMALGHNLSS SSGSAITSVR GGRYGIPRNS PTPMDEQQRV
     QYNQMLPGRN IQQSISVTGT LSGSDHGRML PGGNGIGIMG GINKAMAMSR PGFQGLASPS
     MLNSGSMISS SMVGMPSPVN MHSGVGPGPG NSILRPHETL HMMRPGHNPE HQRQMMVPEL
     QMPVTQGNSQ GIPALCGLSS SFSNQTTPAV QPYPGHAQQS HQLSQQQSHL SNPRPHLQGP
     SHTNSQQQTY AVRLAKERQM QQRYLQHQQQ LAASNALLPH VQAKSQLSIS STPLQNNSQV
     QPQNSSQQVP HSPITPSSPL TPMSSQLQQQ KLHQSQPGFS RNPPASGLTN QVAKQRPQHP
     PQQPPPQQQY QQSGRQHPNQ RHNVQSQQQA KLMKGMGRGS MLVHPNLSVD ASHLSGLSLP
     VGSQTGEKGD QILHMMQGQN IYPGSGLNPN QPSKPLGHTH SSNHSQLQQK LHSGSPTTSS
     KQLHIPSDTK AQAQVSPVSS GQLLSSPPPA VIASNQHQLQ PQSQSKKINH TQTNVQRILP
     LNHPVHSESL KSDPIQADQQ PANSFCKGSA CATVTQSCMD PVTAVPVIAT VSSQWKAAES
     PFDSTVNNQT TQMSSLGSAP AGNSTGNEQP TISQGLEPRS VSLTCHAHNS DTQWQKRQVQ
     PLQQSSQPIL SQQPYQTEQQ QQHEKEEYSP KDIVLQPQQH MPHLQSGQNS MFIQPPNSKV
     E
//
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